Purification and characterization of acid trehalase from muscle of Ascaris suum (Nematoda) |
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Authors: | Dmitryjuk Małgorzata Zółtowska Krystyna |
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Affiliation: | Department of Biochemistry, Faculty of Biology, University of Warmia and Mazury, Oczapowskiego 1A, Olsztyn 10-957, Poland. dmitm@matman.uwm.edu.pl |
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Abstract: | Acid trehalase (EC 3.2.1.28) was isolated from muscle of Ascaris suum by fractionating with ammonium sulfate, acetone and column chromatography on DEAE-cellulose and phenyl sepharose CL-4B. The purified homogeneous preparation of native acid trehalase exhibited a molecular mass of 76 kDa and of 38 kDa on SDS-PAGE. The enzyme has the optimum pH 4.9, pI 4.3, Km of 6.6 mM and Vmax=34.5 nM min(-1) x mg(-1). Besides trehalose, it hydrolyses sucrose, isomaltose and maltose and, to a lesser degree melezitose, and it does not act on cellobiose and lactose. Acid trehalase was activated by MgCl2, KNO3, NaCl, CaCl2, CH2ICOOH and p-chloromercuribenzoate and inhibited by EDTA, ZnSO4 and FeCl3. |
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